English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Evidence for a Role of VIPP1 in the Structural Organization of the Photosynthetic Apparatus in Chlamydomonas

Nordhues, A., Schöttler, M. A., Unger, A. K., Geimer, S., Schoenfelder, S., Schmollinger, S., et al. (2012). Evidence for a Role of VIPP1 in the Structural Organization of the Photosynthetic Apparatus in Chlamydomonas. The Plant Cell, 24(2), 637-659. doi:10.1105/tpc.111.092692.

Item is

Files

show Files
hide Files
:
Nordhues-2012-Evidence for a Role.pdf (Any fulltext), 3MB
Name:
Nordhues-2012-Evidence for a Role.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Nordhues, A.1, Author           
Schöttler, M. A.2, Author           
Unger, A. K.3, Author
Geimer, S.3, Author
Schoenfelder, S.1, Author           
Schmollinger, S.1, Author           
Ruetgers, M.1, Author           
Finazzi, G.3, Author
Soppa, B.3, Author
Sommer, F.1, Author           
Muehlhaus, T.1, Author           
Roach, T.3, Author
Krieger-Liszkay, A.3, Author
Lokstein , H.3, Author
Crespo, J. L.3, Author
Schroda, M.1, Author           
Affiliations:
1Plant Molecular Chaperone Networks and Stress, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753312              
2Photosynthesis Research, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753323              
3External Organizations, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: The vesicle-inducing protein in plastids (VIPP1) was suggested to play a role in thylakoid membrane formation via membrane vesicles. As this functional assignment is under debate, we investigated the function of VIPP1 in Chlamydomonas reinhardtii. Using immunofluorescence, we localized VIPP1 to distinct spots within the chloroplast. In VIPP1-RNA interference/artificial microRNA cells, we consistently observed aberrant, prolamellar body-like structures at the origin of multiple thylakoid membrane layers, which appear to coincide with the immunofluorescent VIPP1 spots and suggest a defect in thylakoid membrane biogenesis. Accordingly, using quantitative shotgun proteomics, we found that unstressed vipp1 mutant cells accumulate 14 to 20% less photosystems, cytochrome b(6)f complex, and ATP synthase but 30% more light-harvesting complex II than control cells, while complex assembly, thylakoid membrane ultrastructure, and bulk lipid composition appeared unaltered. Photosystems in vipp1 mutants are sensitive to high light, which coincides with a lowered midpoint potential of the Q(A)/Q(A)(-) redox couple and increased thermosensitivity of photosystem II (PSII), suggesting structural defects in PSII. Moreover, swollen thylakoids, despite reduced membrane energization, in vipp1 mutants grown on ammonium suggest defects in the supermolecular organization of thylakoid membrane complexes. Overall, our data suggest a role of VIPP1 in the biogenesis/assembly of thylakoid membrane core complexes, most likely by supplying structural lipids.

Details

show
hide
Language(s): eng - English
 Dates: 2012-02-072012
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 24 (2) Sequence Number: - Start / End Page: 637 - 659 Identifier: Other: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X